Camadan, YaseminCicek, BakiAdem, SevkiCalisir, UmitAkkemik, Ebru2024-12-242024-12-2420220739-11021538-0254https://doi.org/10.1080/07391102.2021.1892527https://hdl.handle.net/20.500.12604/6941Carbonic anhydrases (CAs, EC4.2.1.1) are metalloenzymes that catalyse reversible hydration reaction of carbon dioxide to bicarbonate and protons. In recent years, there has been a great interest in inhibitors/activators of carbonic anhydrase isoenzymes. Therefore, we investigated the effects of four different carbazole Schiff base derivatives, which are believed to have a potential to be used as a drug, on human carbonic anhydrase (hCA) isoenzymes I and II under in vitro conditions. The IC50 values of carbazole Schiff base derivatives were found to be in the range of 32.09-151.2 mu M for hCA isoenzyme I and 21.82-40.54 mu M for hCA isoenzyme II. Among all compounds, (E)-3-(((9-Octyl-9H-carbazole-3-yl)imino)methyl)benzene-1,2-diol (C3) had the strongest inhibitory effect on hCA isoenzyme II. It was determined that 2,3,4-trimethoxy and 4-hydroxy phenyl containing carbazole compounds have selective inhibition against hCA II isoenzyme. Docking studies were performed against hCA I and II receptors using induced-fit docking method. The compounds had affinity scores varying from -7.74 +/- 0.27 to -6.27 +/- 0.07 kcal/mol for hCA I and from -8.04 +/- 0.17 to -7.27 +/- 0.18 kcal/mol for hCA II. Communicated by Ramaswamy H. Sarmaeninfo:eu-repo/semantics/closedAccessCarbazolecarbonic anhydrasedockingesterase activityinhibitionSchiff basesArticle401569656973Q1WOS:000623962400001Q12-s2.0-851018835743364544110.1080/07391102.2021.1892527